메뉴 건너뛰기




Volumn 2011, Issue 1, 2011, Pages

Characterization of the recombinant thermostable lipase (Pf2001) from pyrococcus furiosus: Effects of thioredoxin fusion tag and triton X-100

Author keywords

[No Author keywords available]

Indexed keywords

EDETIC ACID; EGTAZIC ACID; HYBRID PROTEIN; RECOMBINANT ENZYME; THIOREDOXIN; TRIACYLGLYCEROL LIPASE; TRITON X 100;

EID: 84869039652     PISSN: 20900406     EISSN: 20900414     Source Type: Journal    
DOI: 10.4061/2011/316939     Document Type: Article
Times cited : (29)

References (23)
  • 1
    • 0036890248 scopus 로고    scopus 로고
    • The production of biocatalysts and biomolecules from extremophiles
    • DOI 10.1016/S0167-7799(02)02073-5, PII S0167779902020735
    • Schiraldi C., De Rosa M., The production of biocatalysts and biomolecules from extremophiles. Trends in Biotechnology 2002 20 12 515 521 2-s2.0-0036890248 10.1016/S0167-7799(02)02073-5 (Pubitemid 35356406)
    • (2002) Trends in Biotechnology , vol.20 , Issue.12 , pp. 515-521
    • Schiraldi, C.1    De Rosa, M.2
  • 2
    • 0032142867 scopus 로고    scopus 로고
    • Thermozymes: Biotechnology and structure-function relationships
    • DOI 10.1007/s007920050058
    • Zeikus J. G., Vieille C., Savchenko A., Thermozymes: biotechnology and structure-function relationships. Extremophiles 1998 2 3 179 183 2-s2.0-0032142867 10.1007/s007920050058 (Pubitemid 28407997)
    • (1998) Extremophiles , vol.2 , Issue.3 , pp. 179-183
    • Zeikus, J.G.1    Vieille, C.2    Savchenko, A.3
  • 3
    • 0036234420 scopus 로고    scopus 로고
    • Microbial carboxyl esterases: Classification, properties and application in biocatalysis
    • DOI 10.1016/S0168-6445(01)00075-4, PII S0168644501000754
    • Bornscheuer U. T., Microbial carboxyl esterases: classification, properties and application in biocatalysis. FEMS Microbiology Reviews 2002 26 1 73 81 2-s2.0-0036234420 10.1016/S0168-6445(01)00075-4 (Pubitemid 34454776)
    • (2002) FEMS Microbiology Reviews , vol.26 , Issue.1 , pp. 73-81
    • Bornscheuer, U.T.1
  • 4
    • 0036827458 scopus 로고    scopus 로고
    • Lipases and lipase-catalyzed esterification reactions in nonaqueous media
    • 2-s2.0-0036827458 10.1081/CR-120015481
    • Krishna H. S., Karanth N. G., Lipases and lipase-catalyzed esterification reactions in nonaqueous media. Catalysis Reviews 2002 44 4 499 591 2-s2.0-0036827458 10.1081/CR-120015481
    • (2002) Catalysis Reviews , vol.44 , Issue.4 , pp. 499-591
    • Krishna, H.S.1    Karanth, N.G.2
  • 5
    • 78951490005 scopus 로고    scopus 로고
    • Efficient kinetic resolution of (±)-1,2-O-isopropylidene-3,6-di-O- benzyl-myo-inositol with the lipase B of Candida antarctica
    • abcsimas@nppn.ufr.br 10.1016/j.tetasy.2010.12.006
    • Cunha A. G., da Silva A. A. T., da Silva A. J. R., Tinoco L. W., Almeida R. V., De Alencastro R. B., Simas A. B.C., abcsimas@nppn.ufr.br Freire D. M.G., Efficient kinetic resolution of (±)-1,2-O-isopropylidene-3,6-di-O- benzyl-myo-inositol with the lipase B of Candida antarctica. Tetrahedron Asymmetry 2010 21 24 2899 2903 10.1016/j.tetasy.2010.12.006
    • (2010) Tetrahedron Asymmetry , vol.21 , Issue.24 , pp. 2899-2903
    • Cunha, A.G.1    Da Silva, A.A.T.2    Da Silva, A.J.R.3    Tinoco, L.W.4    Almeida, R.V.5    De Alencastro, R.B.6    Simas, A.B.C.7    Freire, D.M.G.8
  • 6
    • 0036669430 scopus 로고    scopus 로고
    • The use of enzymes in the chemical industry in Europe
    • DOI 10.1016/S0958-1669(02)00336-1
    • Schmid A., Hollmann F., Park J. B., Bühler B., The use of enzymes in the chemical industry in Europe. Current Opinion in Biotechnology 2002 13 4 359 366 2-s2.0-0036669430 10.1016/S0958-1669(02)00336-1 (Pubitemid 35254095)
    • (2002) Current Opinion in Biotechnology , vol.13 , Issue.4 , pp. 359-366
    • Schmid, A.1    Hollmann, F.2    Park, J.B.3    Buhler, B.4
  • 7
    • 17944374832 scopus 로고    scopus 로고
    • Production and applications of esterases
    • DOI 10.1007/s00253-004-1840-y
    • Panda T., Gowrishankar B. S., Production and applications of esterases. Applied Microbiology and Biotechnology 2005 67 2 160 169 2-s2.0-17944374832 10.1007/s00253-004-1840-y (Pubitemid 40598020)
    • (2005) Applied Microbiology and Biotechnology , vol.67 , Issue.2 , pp. 160-169
    • Panda, T.1    Gowrishankar, B.S.2
  • 8
    • 77954386384 scopus 로고    scopus 로고
    • Biodiesel production with immobilized lipase: A review
    • 2-s2.0-77954386384 10.1016/j.biotechadv.2010.05.012
    • Tan T., Lu J., Nie K., Deng L., Wang F., Biodiesel production with immobilized lipase: a review. Biotechnology Advances 2010 28 5 628 634 2-s2.0-77954386384 10.1016/j.biotechadv.2010.05.012
    • (2010) Biotechnology Advances , vol.28 , Issue.5 , pp. 628-634
    • Tan, T.1    Lu, J.2    Nie, K.3    Deng, L.4    Wang, F.5
  • 9
    • 33745841316 scopus 로고    scopus 로고
    • A review on hydrolytic enzymes in the treatment of wastewater with high oil and grease content
    • DOI 10.1016/j.biortech.2006.02.030, PII S0960852406000848
    • Cammarota M. C., Freire D. M. G., A review on hydrolytic enzymes in the treatment of wastewater with high oil and grease content. Bioresource Technology 2006 97 17 2195 2210 2-s2.0-33745841316 10.1016/j.biortech.2006.02.030 (Pubitemid 44038375)
    • (2006) Bioresource Technology , vol.97 , Issue.17 , pp. 2195-2210
    • Cammarota, M.C.1    Freire, D.M.G.2
  • 10
    • 33745936224 scopus 로고    scopus 로고
    • Cloning, expression, partial characterization and structural modeling of a novel esterase from Pyrococcus furiosus
    • DOI 10.1016/j.enzmictec.2006.02.021, PII S0141022906000895
    • Almeida R. V., Alquéres S. M. C., Larentis A. L., Rössle S. C., Cardoso A. M., Almeida W. I., Bisch P. M., Alves T. L. M., Martins O. B., Cloning, expression, partial characterization and structural modeling of a novel esterase from Pyrococcus furiosus. Enzyme and Microbial Technology 2006 39 5 1128 1136 2-s2.0-33745936224 10.1016/j.enzmictec.2006.02.021 (Pubitemid 44062666)
    • (2006) Enzyme and Microbial Technology , vol.39 , Issue.5 , pp. 1128-1136
    • Almeida, R.V.1    Alqueres, S.M.C.2    Larentis, A.L.3    Rossle, S.C.4    Cardoso, A.M.5    Almeida, W.I.6    Bisch, P.M.7    Alves, T.L.M.8    Martins, O.B.9
  • 11
    • 41549120002 scopus 로고    scopus 로고
    • Immobilization of a recombinant thermostable esterase (Pf2001) from Pyrococcus furiosus on microporous polypropylene: Isotherms, hyperactivation and purification
    • 2-s2.0-41549120002 10.1016/j.bej.2007.09.019
    • Almeida R. V., Branco R. V., Peixoto B., Lima C., Alqueres S. M. C., Martins O. B., Antunes O. A. C., Freire D. M. G., Immobilization of a recombinant thermostable esterase (Pf2001) from Pyrococcus furiosus on microporous polypropylene: isotherms, hyperactivation and purification. Biochemical Engineering Journal 2008 39 3 531 537 2-s2.0-41549120002 10.1016/j.bej.2007.09.019
    • (2008) Biochemical Engineering Journal , vol.39 , Issue.3 , pp. 531-537
    • Almeida, R.V.1    Branco, R.V.2    Peixoto, B.3    Lima, C.4    Alqueres, S.M.C.5    Martins, O.B.6    Antunes, O.A.C.7    Freire, D.M.G.8
  • 12
    • 79958089022 scopus 로고    scopus 로고
    • Immobilization and characterization of a recombinant thermostable lipase (Pf2001) from Pyrococcus furiosus on supports with different degrees of hydrophobicity
    • 10.4061/2010/180418 180418
    • Branco R. V., Gutarra M. L. E., Freire D. M. G., Almeida R. V., Immobilization and characterization of a recombinant thermostable lipase (Pf2001) from Pyrococcus furiosus on supports with different degrees of hydrophobicity. Enzyme Research 2010 2010 1 8 10.4061/2010/180418 180418
    • (2010) Enzyme Research , vol.2010 , pp. 1-8
    • Branco, R.V.1    Gutarra, M.L.E.2    Freire, D.M.G.3    Almeida, R.V.4
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 2-s2.0-0014949207 10.1038/227680a0
    • Laemmli U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970 227 680 685 2-s2.0-0014949207 10.1038/227680a0
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0038353703 scopus 로고    scopus 로고
    • Use of methylumbeliferyl-derivative substrates for lipase activity characterization
    • DOI 10.1016/S1381-1177(03)00048-1
    • Prim N., Sánchez M., Ruiz C., Pastor F. I. J., Diaz P., Use of methylumbeliferyl-derivative substrates for lipase activity characterization. Journal of Molecular Catalysis B: Enzymatic 2003 22 5-6 339 346 2-s2.0-0038353703 10.1016/S1381-1177(03)00048-1 (Pubitemid 36802034)
    • (2003) Journal of Molecular Catalysis B: Enzymatic , vol.22 , Issue.5-6 , pp. 339-346
    • Prim, N.1    Sanchez, M.2    Ruiz, C.3    Pastor, F.I.J.4    Diaz, P.5
  • 15
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 2-s2.0-0017184389
    • Bradford M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 1976 72 1-2 248 254 2-s2.0-0017184389
    • (1976) Analytical Biochemistry , vol.72 , Issue.1-2 , pp. 248-254
    • Bradford, M.M.1
  • 16
    • 14744292185 scopus 로고
    • A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm
    • DOI 10.1038/nbt0293-187
    • LaVallie E. D., DiBlasio E. A., Kovacic S., Grant K. L., Schendel P. F., McCoy J. M., A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm. Nature Biotechnology 1993 11 2 187 193 2-s2.0-14744292185 (Pubitemid 23056045)
    • (1993) Bio/Technology , vol.11 , Issue.2 , pp. 187-193
    • LaVallie, E.R.1    DiBlasio, E.A.2    Kovacic, S.3    Grant, K.L.4    Schendel, P.F.5    McCoy, J.M.6
  • 17
    • 0034961587 scopus 로고    scopus 로고
    • A single point mutation (Glu85Arg) increases the stability of the thioredoxin from Escherichia coli
    • Pedoni E., Saviano M., Rossi M., Bartolucci S., A single point mutation (Glu85Arg) increases the stability of the thioredoxin from E. coli. Protein Engineering 2001 14 4 255 260 2-s2.0-0034961587 (Pubitemid 32587271)
    • (2001) Protein Engineering , vol.14 , Issue.4 , pp. 255-260
    • Pedone, E.1    Saviano, M.2    Rossi, M.3    Bartolucci, S.4
  • 18
    • 0035852885 scopus 로고    scopus 로고
    • How do lipases and esterases work: The electrostatic contribution
    • DOI 10.1016/S0168-1656(00)00360-6, PII S0168165600003606
    • Neves Petersen M. T., Fojan P., Petersen S. B., How do lipases and esterases work. Journal of Biotechnology 2001 85 2 115 147 2-s2.0-0035852885 10.1016/S0168-1656(00)00360-6 (Pubitemid 32124718)
    • (2001) Journal of Biotechnology , vol.85 , Issue.2 , pp. 115-147
    • Neves Petersen, M.T.1    Fojan, P.2    Petersen, S.B.3
  • 19
    • 0031613603 scopus 로고    scopus 로고
    • Gene cloning and characterization of thermostable lipase from Bacillus stearothermophilus L1
    • 2-s2.0-0031613603
    • Kim H. K., Park S. Y., Lee J. K., Oh T. K., Gene cloning and characterization of thermostable lipase from Bacillus stearothermophilus L1. Bioscience, Biotechnology and Biochemistry 1998 62 1 66 71 2-s2.0-0031613603
    • (1998) Bioscience, Biotechnology and Biochemistry , vol.62 , Issue.1 , pp. 66-71
    • Kim, H.K.1    Park, S.Y.2    Lee, J.K.3    Oh, T.K.4
  • 20
    • 33751542136 scopus 로고    scopus 로고
    • A novel esterase from Ralstonia sp. M1: Gene cloning, sequencing, high-level expression and characterization
    • DOI 10.1016/j.pep.2006.06.009, PII S1046592806001847
    • Quyen D. T., Dao T. T., Thanh Nguyen S. L. T., A novel esterase from Ralstonia sp. M1: gene cloning, sequencing, high-level expression and characterization. Protein Expression and Purification 2007 51 2 133 140 2-s2.0-33751542136 10.1016/j.pep.2006.06.009 (Pubitemid 44830116)
    • (2007) Protein Expression and Purification , vol.51 , Issue.2 , pp. 133-140
    • Quyen, D.T.1    Dao, T.T.2    Thanh Nguyen, S.L.3
  • 21
    • 33748414191 scopus 로고    scopus 로고
    • Efficient production of active recombinant Candida rugosa LIP3 lipase in Pichia pastoris and biochemical characterization of the purified enzyme
    • DOI 10.1021/jf060835e
    • Chang S., Lee G., Shaw J., Efficient production of active recombinant Candida rugosa LIP3 lipase in Pichia pastoris and biochemical characterization of the purified enzyme. Journal of Agricultural and Food Chemistry 2006 54 16 5831 5838 2-s2.0-33748414191 10.1021/jf060835e (Pubitemid 44342211)
    • (2006) Journal of Agricultural and Food Chemistry , vol.54 , Issue.16 , pp. 5831-5838
    • Chang, S.-W.1    Lee, G.-C.2    Shaw, J.-F.3
  • 22
    • 33744478896 scopus 로고    scopus 로고
    • Images in cardiology: Obstructed left coronary cusp as a cause of left main coronary artery obstruction and severe aortic regurgitation
    • DOI 10.1016/j.bbagen.2006.01.009
    • Park Y. J., Choi S. Y., Lee H. B., A carboxylesterase from the thermoacidophilic archaeon Sulfolobus solfataricus P1; purification, characterization, and expression. Biochimica et Biophysica Acta 2006 1760 5 820 828 2-s2.0-33646092557 10.1016/j.bbagen.2006.01.009 (Pubitemid 43799220)
    • (2006) Heart , vol.92 , Issue.6 , pp. 820
    • Park, J.-H.1    Seo, Y.H.2    Kim, K.S.3
  • 23
    • 0030873134 scopus 로고    scopus 로고
    • Aspartate transcarbamylase from the deep-sea hyperthermophilic archaeon Pyrococcus abyssi: Genetic organization, structure, and expression in Escherichia coli
    • Purcarea C., Hervé G., Ladjimi M. M., Cunin R., Aspartate transcarbamylase from the deep-sea hyperthermophilic archaeon Pyrococcus abyssi: genetic organization, structure, and expression in Escherichia coli. Journal of Bacteriology 1997 179 13 4143 4157 2-s2.0-0030873134 (Pubitemid 27291042)
    • (1997) Journal of Bacteriology , vol.179 , Issue.13 , pp. 4143-4157
    • Purcarea, C.1    Herve, G.2    Ladjimi, M.M.3    Cunin, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.